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Information on EC 2.7.7.50 - mRNA guanylyltransferase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.50 mRNA guanylyltransferase
IUBMB Comments
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
d1 protein, guanylyltransferase, capping enzyme, mrna capping enzyme, rna guanylyltransferase, mrna guanylyltransferase, prntase, rna capping enzyme, mrna-cap, mrna-capping enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
capping enzyme
-
Ceg1
-
-
-
-
GTase
-
-
guanylyltransferase
-
-
messenger RNA guanylyltransferase
-
-
-
-
mRNA capping enzyme
-
-
protein lambda2
-
-
-
-
RNGTT
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP:mRNA guanylyltransferase
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
56941-23-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
no activity
-
-
?
GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
show the reaction diagram
-
-
-
-
?
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
-
-
-
?
GTP + diphosphate terminated poly(A) with an average chain length of 2000 nucleotides
?
show the reaction diagram
-
-
-
-
?
GTP + diphosphate-ended poly(A)
?
show the reaction diagram
-
-
-
-
?
GTP + lambdac17RNA
?
show the reaction diagram
-
-
-
-
?
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
show the reaction diagram
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
show the reaction diagram
-
-
-
ir
GTP + ppp(5')ApG
G(5')pppp(5')ApG + diphosphate
show the reaction diagram
-
-
-
-
ir
GTP + ppp(5')ApGp
G(5')pppp(5')ApGp + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
ir
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
show the reaction diagram
-
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
ir
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
hydrogen peroxide
-
inactivates the enzyme directly through irreversible oxidation of Cys126
mizoribine 5'-phosphate
compound can inhibit the formation of the RNA cap structure catalyzed by human capping enzyme. In the presence of mizoribine 5'-phosphate, the RNA 5'-triphosphatase activity appears to be relatively unaffected while the RNA guanylyltransferase activity is inhibited. Mizoribine 5'-phosphate is a non-competitive inhibitor that likely targets an allosteric site
N-ethylmaleimide
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
diphosphate terminated poly(A) with an average chain length of 2000 nucleotides
-
-
-
0.000019
diphosphate-ended poly(A)
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pH 7.5, 37°C
-
0.0011
GTP
-
pH 7.5, 37°C
0.00014
lambdac17RNA
-
pH 7.5, 37°C
-
0.000285
pp(5')ApGp
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000066
-
-
0.00007
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
pH 6.5: about 45% of activity maximum, pH 8.5: about 15% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MCE1_HUMAN
597
0
68557
Swiss-Prot
Mitochondrion (Reliability: 3)
B4DSJ8_HUMAN
514
0
59084
TrEMBL
other Location (Reliability: 1)
B4DIQ0_HUMAN
568
0
65220
TrEMBL
other Location (Reliability: 2)
B2R623_HUMAN
597
0
68485
TrEMBL
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48500
-
sucrose density gradient sedimentation
69000
x * 69000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of residues 229-567, comprising the minimum enzymatically active human guanylyltransferase domain, to 3.0 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D532A
inactive
E234A
mutation does not inhibit the formation of the phosphoamide intermediate
K458A
inactive
K460A
inactive
K533A
inactive
R528A
poor activity
R530A
inactive
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable after a few cycles of freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stable for at least 9 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Mono S column chromatography
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recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
expressed in Escherichia coli DE3 cells
-
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Groner, Y.; Aviv, H.
Methylation and capping of RNA polymerase II primary transcripts by HeLa nuclear homogenates
Biochemistry
17
977-982
1978
Homo sapiens
Manually annotated by BRENDA team
Shuman, S.; Hurwitz, J.
Capping enzyme
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
15
245-265
1982
Homo sapiens, Rattus norvegicus, Vaccinia virus
-
Manually annotated by BRENDA team
Venkatesan, S.; Gershowitz, A.; Moss, B.
Purification and characterization of mRNA guanylyltransferase from HeLa cell nuclei
J. Biol. Chem.
255
2829-2834
1980
Homo sapiens
Manually annotated by BRENDA team
Vankatesan, S.; Moss, B.
Donor and acceptor specificities of HeLa cell mRNA guanylyltransferase
J. Biol. Chem.
255
2835-2842
1990
Homo sapiens
Manually annotated by BRENDA team
Yue, Z.; Maldonado, E.; Pillutla, R.; Cho, H.; Reinberg, D.; Shatkin, A.J.
Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
Proc. Natl. Acad. Sci. USA
94
12898-12903
1997
Mus musculus (O55236), Mus musculus, Homo sapiens (O60942), Homo sapiens
Manually annotated by BRENDA team
Picard-Jean, F.; Bougie, I.; Shuto, S.; Bisaillon, M.
The immunosuppressive agent mizoribine monophosphate is an inhibitor of the human RNA capping enzyme
PLoS ONE
8
e54621
2013
Homo sapiens (O60942), Homo sapiens
Manually annotated by BRENDA team
Chu, C.; Das, K.; Tyminski, J.R.; Bauman, J.D.; Guan, R.; Qiu, W.; Montelione, G.T.; Arnold, E.; Shatkin, A.J.
Structure of the guanylyltransferase domain of human mRNA capping enzyme
Proc. Natl. Acad. Sci. USA
108
10104-10108
2011
Homo sapiens (O60942), Homo sapiens
Manually annotated by BRENDA team
Mullen, N.J.; Price, D.H.
Hydrogen peroxide yields mechanistic insights into human mRNA capping enzyme function
PLoS ONE
12
e0186423
2017
Homo sapiens
Manually annotated by BRENDA team